Protein Structure and Function

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 Learning objectives-protein structure and
function
• Know the definitions of primary, secondary, tertiary, and
quaternary structures or protein
• Understand the differences between globular and fibrous
proteins
• Know the forces that stabilize these structures
• Understand the type of bonds that stabilize these structures
• Understand that certain changes in protein structure can
change the structure and function of protein

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 Peptide Bond Is Rigid and Planar

C H

C N
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 Terminology
• Conformation – spatial arrangement of
atoms in a protein
• Native conformation – conformation of
functional protein

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Alpha Helix

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 Beta-Sheets

• Beta-sheets
formed from
multiple side-by-
side beta-strands.
• Can be in parallel or
anti-parallel
configuration
• Anti-parallel beta-
sheets more stable

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Bonds holding the tertiary structure of
Proteins

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 Protein Function
• Catalysis – enzymes
• Structural – keratin
• Transport – hemoglobin
• Trans-membrane transport – Na+/K+ ATPases
• Toxins – rattle snake venom, ricin
• Contractile function – actin, myosin
• Hormones – insulin
• Storage Proteins – seeds and eggs
• Defensive proteins – antibodies

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 Protein Classification
• One polypeptide chain - monomeric protein
• More than one - multimeric protein
Homomultimer – all one kind of chain
Heteromultimer - two or more different chains

(e.g. Hemoglobin is a heterotetramer. It has two alpha

chains and two beta chains).

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 Protein Classification
Fibrous –
1) polypeptides arranged in long strands or
sheets
2) water insoluble (lots of hydrophobic AA’s)
3) strong but flexible
4) Structural (keratin, collagen)

Globular –
1) polypeptide chains folded into spherical or
globular form
2) water soluble
3) contain several types of secondary structure
4) diverse functions (enzymes, regulatory
proteins)
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 Protein Classification
• Simple – composed only of amino acid residues

• Conjugated – contain prosthetic groups

(metal ions, co-factors, lipids, carbohydrates)
Example: Hemoglobin – Heme

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 Diseases caused by changes in protein structure

• spongiform encephalopathy (BSE or mad cow disease) seen

in cattle and livestock and Creutzfeldt-Jakob disease (CJD)
seen in humans.
• Sickle Cell Anemia – single amino acid change in hemoglobin
related to disease
• Osteoarthritis – single amino acid change in collagen protein
causes joint damage

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 Prion Misfolding

Prion protein misfolding 21

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Prion propagation

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Sickle cell anemia

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 Mutations in a- or b-globin
genes can cause disease state
• Sickle cell anemia – E6 to
V6
• Causes V6 to bind to
hydrophobic pocket in
deoxy-Hb
• Polymerizes to form long
filaments
• Cause sickling of cells
• Sickle cell trait offers
advantage against malaria
• Fragile sickle cells can not
support parasite
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